Component
Human carnosinase 1 / CNDP1
Context-specific entity; species, compartment and exposure are stated on each claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
Recombinant human CNDP1 hydrolyzed carnosine, with a reported Km of 1.2 mM.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified human protein expressed in CHO cells.
- limitations
- Kinetic constant is not a plasma threshold.
- nutrient_topic
- Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine
- plain_language
- A separate enzyme breaks the peptide down.
- primary_references
- Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200
Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 44–50
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified human protein expressed in CHO cells. · source_derived_draft · unverified_draft
## carnosine-cndp1-hydrolysis A separate enzyme breaks the peptide down. Recombinant human CNDP1 hydrolyzed carnosine, with a reported Km of 1.2 mM. Model: Purified human protein expressed in CHO cells. Limitations: Kinetic constant is not a plasma threshold. Evidence access: Primary abstract Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200
Complete structured claim and evidenceIntact carnosine became detectable in sampled plasma when ex vivo blood carnosinase activity was inhibited.
Experimental context and source evidence
- availability_state
- biomarker_context Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Human blood-sample handling experiment.
- limitations
- A negative untreated plasma assay cannot prove no absorption occurred.
- nutrient_topic
- Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine
- plain_language
- Breakdown after blood collection can hide the signal.
- primary_references
- Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose. · 1991 · https://pubmed.ncbi.nlm.nih.gov/1910085/ · DOI 10.1113/jphysiol.1991.sp018673
- trigger_kind
- biomarker_context Imported condition classification; unverified.
Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 84–90
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human blood-sample handling experiment. · source_derived_draft · unverified_draft
## carnosine-sample-hydrolysis Breakdown after blood collection can hide the signal. Intact carnosine became detectable in sampled plasma when ex vivo blood carnosinase activity was inhibited. Model: Human blood-sample handling experiment. Limitations: A negative untreated plasma assay cannot prove no absorption occurred. Evidence access: Primary abstract Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose. · 1991 · https://pubmed.ncbi.nlm.nih.gov/1910085/ · DOI 10.1113/jphysiol.1991.sp018673
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.